UBP21_BOVIN
ID UBP21_BOVIN Reviewed; 565 AA.
AC Q2KJ72;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 21;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 21;
DE AltName: Full=Ubiquitin thioesterase 21;
DE AltName: Full=Ubiquitin-specific-processing protease 21;
GN Name=USP21;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinates histone H2A, a specific tag for epigenetic
CC transcriptional repression, thereby acting as a coactivator.
CC Deubiquitination of histone H2A releaves the repression of di- and
CC trimethylation of histone H3 at 'Lys-4', resulting in regulation of
CC transcriptional initiation. Regulates gene expression via histone H2A
CC deubiquitination. Also capable of removing NEDD8 from NEDD8 conjugates
CC but has no effect on Sentrin-1 conjugates. Deubiquitinates BAZ2A/TIP5
CC leading to its stabilization. {ECO:0000250|UniProtKB:Q9UK80}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- SUBUNIT: Interacts with BEND3 and BAZ2A/TIP5.
CC {ECO:0000250|UniProtKB:Q9UK80}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP21 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC105488; AAI05489.1; -; mRNA.
DR RefSeq; NP_001039841.1; NM_001046376.2.
DR AlphaFoldDB; Q2KJ72; -.
DR SMR; Q2KJ72; -.
DR STRING; 9913.ENSBTAP00000029184; -.
DR MEROPS; C19.034; -.
DR PaxDb; Q2KJ72; -.
DR PRIDE; Q2KJ72; -.
DR GeneID; 534273; -.
DR KEGG; bta:534273; -.
DR CTD; 27005; -.
DR eggNOG; KOG1868; Eukaryota.
DR InParanoid; Q2KJ72; -.
DR OrthoDB; 561804at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0019784; F:deNEDDylase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Activator; Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding;
KW Nucleus; Protease; Reference proteome; Thiol protease; Transcription;
KW Transcription regulation; Ubl conjugation pathway; Zinc.
FT CHAIN 1..565
FT /note="Ubiquitin carboxyl-terminal hydrolase 21"
FT /id="PRO_0000367508"
FT DOMAIN 212..558
FT /note="USP"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..152
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 518
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 565 AA; 62619 MW; 6AA35C030406094C CRC64;
MPQASEHRLG RTREPPLNIQ PRVGSKLPFA PRARSKERRN PAPGPNPMLR PLPPRPGPPE
ERLKKLELGR GRTSGPRPSG PLRADHGVPL PGSPPPTVAL PLPSRTNLAR SKSVSSGDLR
PMGIALGGHR GTGELGAALS RLALRPEPPP LRRSTSLRRL GGFPGPPTLF SIRTEPPTPH
GSFHVISARP SEPFYSDDKM AHHTLLLGSG HVGLRNLGNT CFLNALLQCL SSTRPLRDFC
LRRDFRQEVP GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ
DAQEFLKLLM ERLHLEINRR GRRAPPILAS SPAPHPPRLG GALLEEPELS DDDRANLMWK
RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL SLPIPKKGFA GGKVSLRDCF
NLFTKEEELE SENAPVCDRC RQKTRSTKKL TVQRFPRILV LHLNRFSASR GSIKKSSVGV
DFPLQRLSLG DFASDKAGSP VYQLYALCNH SGSVHYGHYT ALCRCQTGWH VYNDSRVSPV
SENQVASSEG YVLFYQLMQE PPRCL
